PDBe 4e28

X-ray diffraction
2.3Å resolution

Structure of human thymidylate synthase in inactive conformation with a novel non-peptidic inhibitor

Released:

Function and Biology Details

Reaction catalysed:
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. 
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 37.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04818 (Residues: 1-313; Coverage: 100%)
Gene names: OK/SW-cl.29, TS, TYMS
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate Synthase, chain A

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P3121
Unit cell:
a: 95.747Å b: 95.747Å c: 82.407Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.229
Expression system: Escherichia coli